Detection of Small, Fast-moving Hæmoglobin Fractions with a Modified Starch-gel Electrophoresis Technique

Nature ◽  
1964 ◽  
Vol 201 (4921) ◽  
pp. 833-834 ◽  
Author(s):  
P. W. HELLEMAN ◽  
H. GARTNER
Keyword(s):  
Gel Electrophoresis ◽  
Fast Moving ◽  
Modified Starch ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Electrophoresis Technique

STARCH GEL ELECTROPHORESIS TECHNIQUE USED WITH ALFALFA AND OTHER Medicago SPECIES

1981 ◽  
Vol 61 (3) ◽  
pp. 745-749 ◽  
Author(s):  
CARLOS F. QUIROS
Keyword(s):  
Enzyme Activity ◽  
Related Species ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Alcohol Dehydrogenases ◽  
Leucine Aminopeptidases ◽  
Starch Gel ◽  
Medicago Sativa L ◽  
Medicago Species ◽  
Electrophoresis Technique

Starch gel electrophoresis is currently used in our laboratory for the study of the genetics and evolution of alfalfa (Medicago sativa L.) and related species. An account is given of this technique, and the staining of the gels for enzyme activity of peroxidases, leucine-aminopeptidases, esterases, and alcohol dehydrogenases.

Separation of Fast-Moving γ-Globulins by Starch-Gel Electrophoresis

Nature ◽  
1959 ◽  
Vol 184 (4701) ◽  
pp. 1800-1801 ◽  
Author(s):  
M. D. POULIK ◽  
W. W. ZUELZER ◽  
R. MEYER
Keyword(s):  
Gel Electrophoresis ◽  
Fast Moving ◽  
Starch Gel Electrophoresis ◽  
Γ Globulins ◽  
Starch Gel

Improving of Starch Gel Electrophoresis Technique by Gamma Irradiation

1977 ◽  
Vol 29 (5) ◽  
pp. 157-160 ◽  
Author(s):  
R. M. A. El Saadany ◽  
F. M. El Saadany ◽  
Y. H. Foda
Keyword(s):  
Gamma Irradiation ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Electrophoresis Technique

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.

Morphological and biochemical systematics of chubs, Nocomis biguttatus and N. micropogon (Pisces: Cyprinidae), in southern Ontario

1981 ◽  
Vol 59 (5) ◽  
pp. 771-775 ◽  
Author(s):  
Moira M. Ferguson ◽  
David L. G. Noakes ◽  
Roy G. Danzmann
Keyword(s):  
Gel Electrophoresis ◽  
Function Analysis ◽  
Morphological Differentiation ◽  
Sexually Dimorphic ◽  
Starch Gel Electrophoresis ◽  
Southern Ontario ◽  
Electrophoretic Mobilities ◽  
Starch Gel ◽  
Respective Species ◽  
Probability Of Misclassification

Examination of 17 presumptive gene loci by starch-gel electrophoresis revealed differential mobilities only at acid phosphatase-1, alcohol dehydrogenase, esterase-1, and phosphoglucomutase between Nocomis biguttatus and N. micropogon. No intraspecific variation was observed for any loci. The genetic identity (I) and genetic distance (D) were 0.874 and 0.134, respectively. The correlation of electrophoretic mobilities and nuptial tubercle pattern in sexually dimorphic males supports the present taxonomic distinction of these species and provides a simple, unambiguous means of identifying any individuals.Stepwise discriminant function analysis of a series of mensural characters was used to compare fish identified as to species by electrophoresis. At best this correctly assigned fish to their respective species in 85.7% of cases, with a probability of misclassification of 0.1335.This study suggests these two are sibling species, based on a comparison of biochemical and morphological differentiation.

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